ISSN:
1432-2242
Keywords:
Key words α-Gliadin
;
Microsatellites
;
Sequence variation
;
Pseudogenes
;
Polyglutamine
Source:
Springer Online Journal Archives 1860-2000
Topics:
Biology
Notes:
Abstract The derived amino-acid sequences of all reported α-gliadin clones are compared and analyzed, and the patterns of sequence change within the α-gliadin family are examined. The most variable sequences are two polyglutamine domains. These two domains are characteristic features of the α-gliadin storage proteins and account for most of the variation in protein size of this otherwise highly conserved protein family. In addition, their encoding DNA sequences form microsatellites. Single-base substitutions in the α-gliadin genes show a preponderance of transitions, including the C to T substitution which contributes to the generation of stop codons, and consequently to the observation that approximately 50% of the α-gliadin genes are pseudogenes. In one unusual gene, a microsatellite has expanded to 321 bp as compared to the normal 36–72 bp, and may result from similar mechanisms that produce polyglutamine-associated genetic diseases in humans. A comparison of the 27 reported sequences show several α-gliadin gene subfamilies, at least some of which are genome specific.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1007/s001220050532
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